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NRC Research Press

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Kinetic studies of unmodified individual Escherichia coli β-galactosidase molecules in free solution

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Interconversion of a pair of active-site residues in Escherichia coli cystathionine γ-synthase, E. coli cystathionine β-lyase, and Saccharomyces cerevisiae cystathionine γ-lyase and development of tools for the investigation of their mechanisms and reaction specificity

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Cysteine 265 Is in the Active Site of, But Is Not Essential for Catalysis by tRNA-Guanine Transglycosylase (TGT) from Escherichia coli

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Active Dimeric Form of Inorganic Pyrophosphatase from Escherichia coli

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